superoxide dismutase
Quick Summary
Superoxide dismutase (SOD) is a metal-containing antioxidant enzyme that plays a crucial role in protecting cells from damage caused by harmful free radicals of oxygen. These free radicals are byproducts of normal metabolic processes. SOD works by converting these harmful oxygen free radicals into oxygen and hydrogen peroxide.1
Molecular oxygen, while essential for life, can also be toxic. During its conversion to water in the body, it can produce intermediates like superoxide (O₂⁻) and hydrogen peroxide (H₂O₂), which can lead to DNA damage and cell death. SOD is a key defense mechanism against these toxic effects.2
Interestingly, mutations in the gene for superoxide dismutase have been linked to a familial form of amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig disease.2
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- amyotrophic lateral sclerosisCauses of ALS
…enzyme known as SOD, or superoxide dismutase, appear to facilitate the destruction of motor neurons by harmful molecules known as free radicals (molecular by-products of normal cell metabolism that can accumulate in and destroy cells). ALS-associated mutations in SOD1 result in the inability of the SOD enzyme to neutralize free…
Read More…enzyme known as SOD, or superoxide dismutase, appear to facilitate the destruction of motor neurons by harmful molecules known as free radicals (molecular by-products of normal cell metabolism that can accumulate in and destroy cells). ALS-associated mutations in SOD1 result in the inability of the SOD enzyme to neutralize free…
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human genetic diseaseMolecular oxygen…from mutations affecting the enzyme superoxide dismutase. The disease is genetically dominant, so that the mutant enzyme causes the disease even when half of the superoxide dismutase present in cells exists in the normal form. Interestingly, most of the mutant variants retain full catalytic activity.
Read More…from mutations affecting the enzyme superoxide dismutase. The disease is genetically dominant, so that the mutant enzyme causes the disease even when half of the superoxide dismutase present in cells exists in the normal form. Interestingly, most of the mutant variants retain full catalytic activity.
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